scholarly journals G‐alpha interacting protein interacting protein, C terminus 1 regulates epileptogenesis by increasing the expression of metabotropic glutamate receptor 7

2021 ◽  
Author(s):  
Yong Liu ◽  
You Wang ◽  
Juan Yang ◽  
Tao Xu ◽  
Changhong Tan ◽  
...  
Keyword(s):  
Glutamate Receptor ◽  
Protein C ◽  
Metabotropic Glutamate Receptor ◽  
Interacting Protein ◽  
Metabotropic Glutamate ◽  
C Terminus

scholarly journals The C Terminus of the Metabotropic Glutamate Receptor Subtypes 2 and 7 Specifies the Receptor Signaling Pathways

2001 ◽  
Vol 276 (49) ◽  
pp. 45800-45805 ◽  
Author(s):  
Julie Perroy ◽  
Gustavo J. Gutierrez ◽  
Vincent Coulon ◽  
Joel Bockaert ◽  
Jean-Pilippe Pin ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Glutamate Receptor ◽  
Metabotropic Glutamate Receptor ◽  
Receptor Subtypes ◽  
Receptor Signaling ◽  
Metabotropic Glutamate ◽  
C Terminus

scholarly journals The C-terminus of the metabotropic glutamate receptor 1b regulates dimerization of the receptor

2008 ◽  
Vol 104 (4) ◽  
pp. 1020-1031 ◽  
Author(s):  
Rosaria Remelli ◽  
Melanie J. Robbins ◽  
R. A. Jeffrey McIlhinney
Keyword(s):  
Glutamate Receptor ◽  
Metabotropic Glutamate Receptor ◽  
Metabotropic Glutamate ◽  
C Terminus

scholarly journals Cannabinoid Receptor Interacting Protein 1a (CRIP1a): Function and Structure

Molecules ◽  
2019 ◽  
Vol 24 (20) ◽  
pp. 3672 ◽  
Author(s):  
William T. Booth ◽  
Noah B. Walker ◽  
W. Todd Lowther ◽  
Allyn C. Howlett
Keyword(s):  
Metabotropic Glutamate Receptor ◽  
Cannabinoid Receptor ◽  
Cb1 Receptor ◽  
Receptor Internalization ◽  
Receptor Interaction ◽  
Interacting Protein ◽  
Receptor Associated Protein ◽  
Metabotropic Glutamate ◽  
C Terminus

Cannabinoid receptor interacting protein 1a (CRIP1a) is an important CB1 cannabinoid receptor-associated protein, first identified from a yeast two-hybrid screen to modulate CB1-mediated N-type Ca2+ currents. In this paper we review studies of CRIP1a function and structure based upon in vitro experiments and computational chemistry, which elucidate the specific mechanisms for the interaction of CRIP1a with CB1 receptors. N18TG2 neuronal cells overexpressing or silencing CRIP1a highlighted the ability of CRIP1 to regulate cyclic adenosine 3′,5′monophosphate (cAMP) production and extracellular signal-regulated kinase (ERK1/2) phosphorylation. These studies indicated that CRIP1a attenuates the G protein signaling cascade through modulating which Gi/o subtypes interact with the CB1 receptor. CRIP1a also attenuates CB1 receptor internalization via β-arrestin, suggesting that CRIP1a competes for β-arrestin binding to the CB1 receptor. Predictions of CRIP1a secondary structure suggest that residues 34-110 are minimally necessary for association with key amino acids within the distal C-terminus of the CB1 receptor, as well as the mGlu8a metabotropic glutamate receptor. These interactions are disrupted through phosphorylation of serines and threonines in these regions. Through investigations of the function and structure of CRIP1a, new pharmacotherapies based upon the CRIP-CB1 receptor interaction can be designed to treat diseases such as epilepsy, motor dysfunctions and schizophrenia.

Are there ionotropic glutamate receptors on the rod bipolar cell of the mouse retina?

1997 ◽  
Vol 14 (1) ◽  
pp. 103-109 ◽  
Author(s):  
Thomas E. Hughes
Keyword(s):  
Glutamate Receptors ◽  
Glutamate Receptor ◽  
Bipolar Cell ◽  
Metabotropic Glutamate Receptor ◽  
Bipolar Cells ◽  
Ionotropic Glutamate Receptors ◽  
Mouse Retina ◽  
Rod Photoreceptor ◽  
Metabotropic Glutamate ◽  
C Terminus

AbstractThere is some evidence that the mammalian rod bipolar cell expresses ionotropic glutamate receptors. This is surprising in light of the strong evidence that the glutamate released by the rod photoreceptor acts upon a metabotropic glutamate receptor-mGluRo-present in the dendrites of the rod bipolar cell. To reexamine the issue of which glutamate receptor subunits may be present on the rod bipolar cell, an immunohistochemical study of acutely dissociated retinal cells was undertaken. Two monoclonal antibodies provided some evidence that GluR2 and/or GluR4, as well as NMDAR1 subunit, are present on the rod bipolar cell. A monoclonal antibody directed against the N-terminus of GluR2 labeled the rod bipolar cells, but two antisera directed against the C-terminus of the same subunit did not. One possible explanation for this discrepancy could be that the rare splice variant GluR2-long, which is endowed with a different C-terminus, could be expressed by the rod bipolar cell. To explore this possibility, RT-PCR was used to amplify the transcripts encoding GluR2 in the neural retina. This revealed that GluR2-long transcripts, with the flop exon, are present.

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